BGS4_SCHPO
ID BGS4_SCHPO Reviewed; 1955 AA.
AC O74475; P78840;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=1,3-beta-glucan synthase component bgs4;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
GN Name=bgs4; ORFNames=SPCC1840.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1681-1955.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-965; SER-969; SER-971 AND
RP THR-976, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA20125.1; -; Genomic_DNA.
DR EMBL; D89189; BAA13851.1; -; mRNA.
DR PIR; T41170; T41170.
DR PIR; T42747; T42747.
DR RefSeq; NP_588501.1; NM_001023491.2.
DR AlphaFoldDB; O74475; -.
DR BioGRID; 275403; 20.
DR STRING; 4896.SPCC1840.02c.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; O74475; -.
DR MaxQB; O74475; -.
DR PaxDb; O74475; -.
DR PRIDE; O74475; -.
DR EnsemblFungi; SPCC1840.02c.1; SPCC1840.02c.1:pep; SPCC1840.02c.
DR GeneID; 2538822; -.
DR KEGG; spo:SPCC1840.02c; -.
DR PomBase; SPCC1840.02c; bgs4.
DR VEuPathDB; FungiDB:SPCC1840.02c; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; O74475; -.
DR OMA; AWTDFFI; -.
DR PhylomeDB; O74475; -.
DR BRENDA; 2.4.1.34; 5613.
DR PRO; PR:O74475; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; NAS:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0035841; C:new growing cell tip; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0000936; C:primary cell septum; IDA:PomBase.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:PomBase.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:1990344; P:secondary cell septum biogenesis; IMP:PomBase.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1955
FT /note="1,3-beta-glucan synthase component bgs4"
FT /id="PRO_0000121724"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1362..1382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1421..1441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1507..1527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1531..1551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1624..1644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1677..1697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1713..1733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1748..1768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1815..1835
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1877..1897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 965
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 976
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 1733
FT /note="F -> W (in Ref. 2; BAA13851)"
FT /evidence="ECO:0000305"
FT CONFLICT 1809
FT /note="A -> D (in Ref. 2; BAA13851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1955 AA; 225187 MW; 4B37A5F0A862E401 CRC64;
MSGNNENVSG ITGHDAVSDD QYAYDSEVYD DQNAYQRQPA DAYSNEEFLD QADYDSMYGE
GYNGYDYPTG VTESYGDEYT PVDTASSGIN QYSTEKGKFT RPSDEYESEY SDYNAQPSDA
NNFYNLRGDG RYNAYDPSSD SLANVYNSVP YGSSPYDFSN SSFVGNSGSG TPLDGDSGSF
YADSANLTNR EPYPAWTPEN ELPLTKEEIE DIFIDLTNKL GFQRDSMRNM YDFFMCLLDS
RASRMTPDQA LLTLHADYIG SDIANYKKWY FASQMDREDA VGLANVGIYG GKVTSIKEKG
KFFSRNKKAP KVVKPPRKSR FKRKKKKEQP EEAEDEYIDV NTDDSLESAE YRWRSHMRSM
TQFERAQQIA LWLLLWGEAN NVRFMPEVIA FLFKCAYDYI ISPEAQNVTE PVPEGYYLDN
IVSPLYQYMH DQQFEIINGK YVRRERPHDQ LIGYDDINQL FWHAEGIARL IFEDGTRLID
IPASERFHRL PEVQWNRAFY KTYYESRSWF HLITNFNRIW VIHFGMFWYF TAFNSPTLYT
KPFHQRDGPK PTGASQWAAV ACTSVVSCII MAAASLCEYL FVPRRFPGSK PIWKRLCIIV
LIAIINLIPI VYIFGFSSKH QQRSGRRIAV GVVAFLMSIA TYVYFSLVPL QSTFGKLSVK
DSRKYLANKY FTSNFAPLKF DNQALSVIIW VCVFTCKFAE SYFFLTLSIR DPIIVLSTMR
PYLCSIYWAG SRLCFVQPRI ILGIMYFTDL ILFFLDTYLW YIIFNTIFSV LRSFVLGISI
LTPWRNIFSR MPQRIYGKIL ATNDMEIKYK PKILISQIWN AIVISMYREH LLSIDHVQRL
LYHQVPAEEG RRTLRTPTFF VSQDDNIVHT TFFPANSEAE RRLSFFAQSL ATPIPEPVPV
DNMPTFTVLI PHYAEKILLS LREIIREEDQ LSRVTLLEYL KQLHPVEWDC FVKDTKILVE
ENAPYENDSV SEKEGTYKSK VDDLPFYCIG FKSAMPEYTL RTRIWASLRS QTLYRTISGF
MNYSRAIKLL YRVENPEIVQ MFGGNTDRLE RELDRMARRK FKLVVSMQRY AKFTKEEYEN
AEFLLRAYPD LQIAYLDEDP PEEEGAEPQL FAALIDGHSE IMENERRRPK YRIRLSGNPI
LGDGKSDNQN MSLPFYRGEY IQLIDANQDN YLEECLKIRS VLAEFEEMET DNVNPYSESA
RERNKHPVAI LGAREYIFSE NIGILGDVAA GKEQTFGTLF SRTLAQIGGK LHYGHPDFLN
GIFMTTRGGV SKAQKGLHVN EDIYAGMNAM LRGGRIKHCE YFQCGKGRDL GFGSILNFNT
KVGTGMGEQM LSREYYYLGT QLQLDRFLSF YFAHPGFHLN NMFIMLSVQL FMVVLINLGA
IYHVVTVCYY NGNQKLSYDT SIVPRGCYQL GPVLSWLKRC VISIFIVFWI SFIPLTVHEL
IERGVWRATK RFFKQIGSFS PLFEVFTCQV YSQAITSDLA YGGARYIGTG RGFATARLPF
SILYSRFAVP SIYIGARFLM MLLFGTMTVW VAHLIYWWVS IMALCVAPFL FNPHQFDWND
FFVDYREFIR WLSRGNSRSH ANSWIGYCRL TRTRITGYKR RVLGQPSDKI SMDTPRAKFT
NVFFSDVLIP ALLAAGAIIP YFFINSQPGN PMFITDPNNP SPYVHDTKTG TNPILRLVII
SLIPIAAGFG MSGFFGGMAC CLGPAFGLCC KKFPSIFAAI AHTIQIFIFI AIFEVCWFLD
GWSLPKTVLA FCAVTAIHRF IFKILTLLCL SREVKQDSAN ISWWSGKWYG KGYGYHAFTL
PAREFVCKAI ELNLFATDFF LGHLLLFFML PVICIPYIDR WHSVLLFWLR PSRQIRPPIF
STKQNRLRKR IVRRYSALYF SILVIFLILI IVPLAAGAEI RQGLTASEAV AKGAVGWNQT
NSSIGSGIIQ PRDTNYTANY SFWYDRYHFE FNTTY
